Evidence map›Paper›PMID 20843012›Full record

ArticleAnalytical chemistry2010

Separation of peptide isomers with variant modified sites by high-resolution differential ion mobility spectrometry.

Alexandre A Shvartsburg, Andrew J Creese, Richard D Smith, Helen J Cooper

Abstract read
In one paragraph

Article in Analytical chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

39 citing papers in PubMed.

  1. Article
  2. FAIMS Enhances the Detection of PTM Crosstalk Sites.Journal of proteome research · 2022
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Ion Mobility Separation of Peptide Isotopomers.Journal of the American Society for Mass Spectrometry · 2016
    Article
  15. Article
  16. To What Extent is FAIMS Beneficial in the Analysis of Proteins?Journal of the American Society for Mass Spectrometry · 2016
    Article
  17. Advances in Mass Spectrometric Tools for Probing Neuropeptides.Annual review of analytical chemistry (Palo Alto, Calif.) · 2015
    Review
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors.

Alexandre A ShvartsburgEnvironmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory, P.O. Box 999, Richland, Washington 99352, USA.
Andrew J Creese
Richard D Smith
Helen J Cooper

Funding

WORKSHOP AND TRAINING ACTIVITIESP41RR018522 · NCRR · BATTELLE PACIFIC NORTHWEST LABORATORIES · PI SMITH, RICHARD D · 2003 to 2011
$25.1M
NCRR NIH HHS P41 RR018522NCRR NIH HHS RR18522Wellcome TrustWellcome Trust 074131
6 · The paper itself

Abstract

Many proteins and proteolytic peptides incorporate the same post-translational modification (PTM) at different sites, creating multiple localization variants with different functions or activities that may coexist in cells. Current analytical methods based on liquid chromatography (LC) followed by tandem mass spectrometry (MS/MS) are challenged by such isomers that often coelute in LC and/or produce nonunique fragment ions. The application of ion mobility spectrometry (IMS) was explored, but success has been limited by insufficient resolution. We show that high-resolution differential ion mobility spectrometry (FAIMS) employing helium-rich gases can readily separate phosphopeptides with variant modification sites. Use of He/N(2) mixtures containing up to 74% He has allowed separating to >95% three monophosphorylated peptides of identical sequence. Similar separation was achieved at 50% He, using an elevated electric field. Bisphosphorylated isomers that differ in only one modification site were separated to the same extent. We anticipate FAIMS capabilities for such separations to extend to other PTMs.

Indexed as

Amino Acid SequenceChromatography, High Pressure LiquidIsomerismMolecular Sequence DataPhosphopeptidesTandem Mass SpectrometryPhosphopeptides

Identifiers

PMID20843012
PMCPMC2973842

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.